5HPZ

type II water soluble Chl binding proteins

5HPZ の概要

• エントリーDOI: 10.2210/pdb5hpz/pdb
• 分子名称: Water-soluble chlorophyll protein, 13'2-hydroxyl-Chlorophyll a (3 entities in total)
• 機能のキーワード: chl spectra in the type ii water soluble chl binding proteins from brassicaceae, chlorophyll binding protein
• 由来する生物種: Brassicaceae (Mustard family); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40106.33

構造登録者

Bednarczyk, D.,Dym, O.,Prabahard, V.,Noy, D. (登録日: 2016-01-21, 公開日: 2016-05-04, 最終更新日: 2024-10-23)

主引用文献

Bednarczyk, D.,Dym, O.,Prabahar, V.,Peleg, Y.,Pike, D.H.,Noy, D.
Fine Tuning of Chlorophyll Spectra by Protein-Induced Ring Deformation.
Angew.Chem.Int.Ed.Engl., 55:6901-6905, 2016

PubMed Abstract: The ability to tune the light-absorption properties of chlorophylls by their protein environment is the key to the robustness and high efficiency of photosynthetic light-harvesting proteins. Unfortunately, the intricacy of the natural complexes makes it very difficult to identify and isolate specific protein-pigment interactions that underlie the spectral-tuning mechanisms. Herein we identify and demonstrate the tuning mechanism of chlorophyll spectra in type II water-soluble chlorophyll binding proteins from Brassicaceae (WSCPs). By comparing the molecular structures of two natural WSCPs we correlate a shift in the chlorophyll red absorption band with deformation of its tetrapyrrole macrocycle that is induced by changing the position of a nearby tryptophan residue. We show by a set of reciprocal point mutations that this change accounts for up to 2/3 of the observed spectral shift between the two natural variants.

PubMed: 27098554
DOI: 10.1002/anie.201512001

実験手法

X-RAY DIFFRACTION (1.96 Å)